Quantitative proteomics reveals the kinetics of trypsin-catalyzed protein digestion

	Quantitative proteomics reveals the kinetics of trypsin-catalyzed protein digestion
	Pan, Yanbo 1,2; Cheng, Kai 1,2; Mao, Jiawei 1,2; Liu, Fangjie 1,2; Liu, Jing 1,2; Ye, Mingliang 1; Zou, Hanfa 1
刊名	analytical and bioanalytical chemistry
	2014-10-01
卷号	406 期号:25 页码:6247-6256
关键词	Trypsin Protein digestion Kinetics Stable isotope dimethyl labeling Mass spectrometry
通讯作者	叶明亮 ; 邹汉法
英文摘要	trypsin is the popular protease to digest proteins into peptides in shotgun proteomics, but few studies have attempted to systematically investigate the kinetics of trypsin-catalyzed protein digestion in proteome samples. in this study, we applied quantitative proteomics via triplex stable isotope dimethyl labeling to investigate the kinetics of trypsin-catalyzed cleavage. it was found that trypsin cleaves the c-terminal to lysine (k) and arginine (r) residues with higher rates for r. and the cleavage sites surrounded by neutral residues could be quickly cut, while those with neighboring charged residues (d/e/k/r) or proline residue (p) could be slowly cut. in a proteome sample, a huge number of proteins with different physical chemical properties coexists. if any type of protein could be preferably digested, then limited digestion could be applied to reduce the sample complexity. however, we found that protein abundance and other physicochemical properties, such as molecular weight (mw), grand average of hydropathicity (gravy), aliphatic index, and isoelectric point (pi) have no notable correlation with digestion priority of proteins.
学科主题	物理化学
WOS标题词	science & technology ; life sciences & biomedicine ; physical sciences
类目[WOS]	biochemical research methods ; chemistry, analytical
研究领域[WOS]	biochemistry & molecular biology ; chemistry
关键词[WOS]	missed cleavage sites ; mass-spectrometry ; label-free ; shotgun proteomics ; phosphoproteome ; quantification ; identification ; hydrolysis ; throughput ; prediction
收录类别	SCI
语种	英语
WOS记录号	WOS:000342224300016
公开日期	2016-05-09
内容类型	期刊论文
源URL	[http://cas-ir.dicp.ac.cn/handle/321008/144525]
专题	大连化学物理研究所_中国科学院大连化学物理研究所
作者单位	1.Chinese Acad Sci, Dalian Inst Chem Phys, Natl Chromatog Res & Anal Ctr, Key Lab Separat Sci Analyt Chem, Dalian 116023, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
推荐引用方式 GB/T 7714	Pan, Yanbo,Cheng, Kai,Mao, Jiawei,et al. Quantitative proteomics reveals the kinetics of trypsin-catalyzed protein digestion[J]. analytical and bioanalytical chemistry,2014,406(25):6247-6256.
APA	Pan, Yanbo.,Cheng, Kai.,Mao, Jiawei.,Liu, Fangjie.,Liu, Jing.,...&Zou, Hanfa.(2014).Quantitative proteomics reveals the kinetics of trypsin-catalyzed protein digestion.analytical and bioanalytical chemistry,406(25),6247-6256.
MLA	Pan, Yanbo,et al."Quantitative proteomics reveals the kinetics of trypsin-catalyzed protein digestion".analytical and bioanalytical chemistry 406.25(2014):6247-6256.